Table 1. Crystallographic statistics.
MAD data | |||
Wavelength (Å) | 0.9794 | 0.9798 | 0.9600 |
Unique refl. (total refl.) | 22 625 (126 675) | 22 692 (128 330) | 22 908 (128 321) |
Resolution (Å) (highest shell) | 50–2.6 (2.69–2.6) | 50–2.6 (2.69–2.6) | 50–2.6 (2.69–2.6) |
Rsym (highest shell) | 0.068 (0.284) | 0.069 (0.272) | 0.067 (0.410) |
〈I〉/〈σ〉 (highest shell) | 18.4 (4.5) | 17.4 (4.8) | 18.8 (3.8) |
Completeness, % (highest shell) | 98.4 (99.6) | 99.4 (100.0) | 99.6 (100.0) |
Mean figure of merit | |||
Before density modification | 0.561 | ||
After density modification | 0.715 | ||
Native data | |||
Wavelength (Å) | 1.1000 | ||
Unique refl. (total refl.) | 20 889 (106 953) | ||
Resolution (Å) (highest shell) | 50–2.1 (2.18–2.1) | ||
Rsym (highest shell) | 0.059 (0.370) | ||
〈I〉/〈σ〉 (highest shell) | 21.8 (2.26) | ||
Completeness, % (highest shell) | 97.5 (92.2) | ||
Refinement | |||
Space group | P31 | ||
Unit cell | a=b=63.135 Å, c=82.589 Å, α=β=90°, γ=120° | ||
Resolution (Å) | 2.1 | ||
Rwork/Rfree | 25.8/29.5% | ||
r.m.s.d. bond lengths (Å) | 0.012 | ||
r.m.s.d. bond angles (deg) | 1.9 | ||
Average B-factors (Å2) | |||
Total | 54.588 | ||
Protein | 54.073 | ||
DNA | 92.251 | ||
Water | 53.418 |